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HEADER HYDROLASE 10-FEB-17 5N4B
TITLE PROLYL OLIGOPEPTIDASE B FROM GALERINA MARGINATA BOUND TO 25MER
TITLE 2 MACROCYCLIZATION SUBSTRATE - S577A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ALPHA-AMANITIN PROPROTEIN;
COMPND 8 CHAIN: D, C;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 3 ORGANISM_TAXID: 109633;
SOURCE 4 GENE: POPB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJ411;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 12 ORGANISM_TAXID: 109633
KEYWDS AMANITIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, MACROCYCLASE,
KEYWDS 2 PEPTIDASE, BETA-PROPELLER, CLOSED FORM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.CZEKSTER,S.A.MCMAHON,H.LUDEWIG,J.H.NAISMITH
REVDAT 1 01-NOV-17 5N4B 0
JRNL AUTH C.M.CZEKSTER,H.LUDEWIG,S.A.MCMAHON,J.H.NAISMITH
JRNL TITL CHARACTERIZATION OF A DUAL FUNCTION MACROCYCLASE ENABLES
JRNL TITL 2 DESIGN AND USE OF EFFICIENT MACROCYCLIZATION SUBSTRATES
JRNL REF NAT COMMUN 2017
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-017-00862-4
REMARK 2
REMARK 2 RESOLUTION. 1.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11RC2_2522: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 288430
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 14680
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.5812 - 4.4729 0.99 9585 538 0.1762 0.1872
REMARK 3 2 4.4729 - 3.5508 1.00 9368 491 0.1390 0.1547
REMARK 3 3 3.5508 - 3.1021 1.00 9275 500 0.1522 0.1714
REMARK 3 4 3.1021 - 2.8185 1.00 9211 540 0.1569 0.1940
REMARK 3 5 2.8185 - 2.6165 1.00 9144 533 0.1544 0.1888
REMARK 3 6 2.6165 - 2.4623 1.00 9234 477 0.1516 0.1796
REMARK 3 7 2.4623 - 2.3390 0.98 8993 502 0.1409 0.1672
REMARK 3 8 2.3390 - 2.2372 1.00 9199 467 0.1395 0.1621
REMARK 3 9 2.2372 - 2.1510 0.99 9099 464 0.1404 0.1695
REMARK 3 10 2.1510 - 2.0768 1.00 9096 496 0.1464 0.1787
REMARK 3 11 2.0768 - 2.0119 0.99 9084 499 0.1430 0.1546
REMARK 3 12 2.0119 - 1.9544 1.00 9080 488 0.1428 0.1804
REMARK 3 13 1.9544 - 1.9029 1.00 9119 485 0.1470 0.1686
REMARK 3 14 1.9029 - 1.8565 1.00 9098 477 0.1536 0.1760
REMARK 3 15 1.8565 - 1.8143 1.00 9103 509 0.1501 0.1896
REMARK 3 16 1.8143 - 1.7757 1.00 9144 491 0.1532 0.1667
REMARK 3 17 1.7757 - 1.7401 1.00 9052 476 0.1541 0.1891
REMARK 3 18 1.7401 - 1.7073 1.00 9093 491 0.1565 0.1895
REMARK 3 19 1.7073 - 1.6768 1.00 9176 462 0.1547 0.1834
REMARK 3 20 1.6768 - 1.6484 1.00 9094 485 0.1541 0.1939
REMARK 3 21 1.6484 - 1.6218 1.00 9088 473 0.1552 0.1880
REMARK 3 22 1.6218 - 1.5968 1.00 9093 466 0.1593 0.1884
REMARK 3 23 1.5968 - 1.5734 1.00 9079 528 0.1616 0.1895
REMARK 3 24 1.5734 - 1.5512 1.00 9096 463 0.1664 0.2070
REMARK 3 25 1.5512 - 1.5302 1.00 9128 461 0.1737 0.2195
REMARK 3 26 1.5302 - 1.5104 1.00 9091 471 0.1822 0.2194
REMARK 3 27 1.5104 - 1.4915 1.00 9066 496 0.1912 0.2281
REMARK 3 28 1.4915 - 1.4735 1.00 9078 469 0.2049 0.2368
REMARK 3 29 1.4735 - 1.4564 1.00 9012 510 0.2197 0.2308
REMARK 3 30 1.4564 - 1.4400 0.96 8772 472 0.2379 0.2624
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.570
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 12184
REMARK 3 ANGLE : 1.216 16590
REMARK 3 CHIRALITY : 0.095 1752
REMARK 3 PLANARITY : 0.009 2166
REMARK 3 DIHEDRAL : 15.165 4409
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 6 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8161 75.6285 19.5001
REMARK 3 T TENSOR
REMARK 3 T11: 0.0565 T22: 0.0384
REMARK 3 T33: 0.0601 T12: 0.0167
REMARK 3 T13: 0.0067 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.2667 L22: -0.0112
REMARK 3 L33: 0.2096 L12: -0.1308
REMARK 3 L13: -0.0252 L23: 0.1500
REMARK 3 S TENSOR
REMARK 3 S11: 0.0282 S12: 0.0161 S13: -0.0498
REMARK 3 S21: 0.0158 S22: -0.0519 S23: -0.0187
REMARK 3 S31: 0.0144 S32: 0.0890 S33: -0.0233
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 403 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3717 68.7912 42.0732
REMARK 3 T TENSOR
REMARK 3 T11: 0.0418 T22: 0.0353
REMARK 3 T33: 0.0437 T12: -0.0059
REMARK 3 T13: 0.0015 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.3840 L22: 0.3382
REMARK 3 L33: 0.2406 L12: 0.0041
REMARK 3 L13: 0.0222 L23: 0.0040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0199 S12: -0.0229 S13: -0.0600
REMARK 3 S21: 0.0028 S22: 0.0023 S23: 0.0002
REMARK 3 S31: 0.0118 S32: -0.0015 S33: 0.1082
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 404 THROUGH 727 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0148 81.8270 18.0305
REMARK 3 T TENSOR
REMARK 3 T11: 0.0541 T22: 0.0408
REMARK 3 T33: 0.0416 T12: 0.0035
REMARK 3 T13: 0.0039 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.2885 L22: 0.1078
REMARK 3 L33: 0.1876 L12: -0.0307
REMARK 3 L13: -0.0107 L23: 0.1286
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0395 S13: 0.0055
REMARK 3 S21: 0.0069 S22: -0.0210 S23: 0.0167
REMARK 3 S31: 0.0146 S32: 0.0043 S33: -0.0671
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 6 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7555 34.8559 27.7264
REMARK 3 T TENSOR
REMARK 3 T11: 0.0571 T22: 0.0561
REMARK 3 T33: 0.0494 T12: -0.0024
REMARK 3 T13: -0.0045 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.2292 L22: -0.0024
REMARK 3 L33: 0.2324 L12: -0.0792
REMARK 3 L13: 0.0827 L23: 0.0183
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: -0.0188 S13: 0.0227
REMARK 3 S21: 0.0032 S22: -0.0342 S23: 0.0095
REMARK 3 S31: -0.0279 S32: -0.0692 S33: -0.0179
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 313 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4212 50.9108 41.9785
REMARK 3 T TENSOR
REMARK 3 T11: 0.0735 T22: 0.0677
REMARK 3 T33: 0.0749 T12: 0.0061
REMARK 3 T13: -0.0096 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.2557 L22: 0.3089
REMARK 3 L33: 0.2180 L12: -0.0344
REMARK 3 L13: -0.0480 L23: 0.0555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: -0.0276 S13: 0.0924
REMARK 3 S21: -0.0151 S22: 0.0122 S23: 0.0073
REMARK 3 S31: -0.0411 S32: -0.0526 S33: -0.0003
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 314 THROUGH 348 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.7361 42.7821 42.4497
REMARK 3 T TENSOR
REMARK 3 T11: 0.0567 T22: 0.0519
REMARK 3 T33: 0.0901 T12: -0.0072
REMARK 3 T13: -0.0134 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 0.0388 L22: 0.0240
REMARK 3 L33: 0.0260 L12: -0.0125
REMARK 3 L13: -0.0007 L23: -0.0127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0270 S12: -0.0105 S13: 0.0923
REMARK 3 S21: 0.0010 S22: 0.0071 S23: -0.0761
REMARK 3 S31: -0.0434 S32: 0.0686 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 349 THROUGH 518 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2812 22.3257 32.9474
REMARK 3 T TENSOR
REMARK 3 T11: 0.0527 T22: 0.0523
REMARK 3 T33: 0.0631 T12: -0.0015
REMARK 3 T13: -0.0098 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.2123 L22: 0.0898
REMARK 3 L33: 0.1899 L12: 0.0236
REMARK 3 L13: 0.0612 L23: 0.1085
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: -0.0236 S13: -0.0366
REMARK 3 S21: 0.0121 S22: -0.0037 S23: -0.0287
REMARK 3 S31: 0.0217 S32: -0.0005 S33: -0.0248
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 519 THROUGH 727 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.7227 35.5258 11.6550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0669 T22: 0.0517
REMARK 3 T33: 0.0474 T12: 0.0059
REMARK 3 T13: -0.0062 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.2452 L22: 0.3434
REMARK 3 L33: 0.2404 L12: -0.0067
REMARK 3 L13: 0.0841 L23: -0.0740
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: 0.0552 S13: 0.0281
REMARK 3 S21: 0.0416 S22: -0.0200 S23: -0.0381
REMARK 3 S31: -0.0467 S32: -0.0170 S33: -0.0467
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 9 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1474 80.8116 24.7975
REMARK 3 T TENSOR
REMARK 3 T11: 0.4009 T22: 0.3359
REMARK 3 T33: 0.4688 T12: 0.0218
REMARK 3 T13: 0.0035 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 0.0095 L22: 0.0036
REMARK 3 L33: 0.0028 L12: -0.0010
REMARK 3 L13: 0.0001 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: 0.0064 S13: -0.0074
REMARK 3 S21: -0.0225 S22: 0.0086 S23: 0.0233
REMARK 3 S31: -0.0062 S32: 0.0029 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 14 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8367 80.9158 39.0362
REMARK 3 T TENSOR
REMARK 3 T11: 0.1231 T22: 0.0890
REMARK 3 T33: 0.1100 T12: -0.0174
REMARK 3 T13: -0.0182 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.0036 L22: 0.0164
REMARK 3 L33: 0.0051 L12: 0.0011
REMARK 3 L13: 0.0012 L23: 0.0117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: -0.0714 S13: -0.0333
REMARK 3 S21: -0.0915 S22: 0.0493 S23: 0.1112
REMARK 3 S31: 0.0073 S32: -0.0342 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 9 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3897 30.5526 25.0252
REMARK 3 T TENSOR
REMARK 3 T11: 0.3801 T22: 0.3340
REMARK 3 T33: 0.4408 T12: 0.0065
REMARK 3 T13: -0.0159 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.0172 L22: 0.0017
REMARK 3 L33: 0.0036 L12: -0.0008
REMARK 3 L13: -0.0008 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: 0.0129 S13: 0.0106
REMARK 3 S21: -0.0221 S22: 0.0058 S23: -0.0063
REMARK 3 S31: 0.0048 S32: 0.0004 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 14 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7090 30.2869 39.1933
REMARK 3 T TENSOR
REMARK 3 T11: 0.1208 T22: 0.1087
REMARK 3 T33: 0.1183 T12: -0.0181
REMARK 3 T13: 0.0140 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 0.0092 L22: 0.0218
REMARK 3 L33: 0.0051 L12: -0.0093
REMARK 3 L13: 0.0014 L23: -0.0116
REMARK 3 S TENSOR
REMARK 3 S11: -0.0883 S12: -0.0357 S13: 0.0435
REMARK 3 S21: -0.0751 S22: 0.0425 S23: -0.1580
REMARK 3 S31: 0.0025 S32: -0.0328 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5N4B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003416.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.961
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 288485
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.440
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1H2Z
REMARK 200
REMARK 200 REMARK: SMALL TILES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG6000, 100 MM BICINE PH 9.0, 60
REMARK 280 MM MAGNESIUM FORMATE, AND 2.42% DMSO, 12.5MM HEXAMMINE COBALT
REMARK 280 CHLORIDE, CRYOPROTECTED WITH 12% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 49.54200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.63250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.35800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.63250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.54200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.35800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 THR A 5
REMARK 465 THR A 728
REMARK 465 VAL A 729
REMARK 465 GLU A 730
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 THR B 5
REMARK 465 THR B 728
REMARK 465 VAL B 729
REMARK 465 GLU B 730
REMARK 465 ILE D 1
REMARK 465 TRP D 2
REMARK 465 GLY D 3
REMARK 465 ILE D 4
REMARK 465 GLY D 5
REMARK 465 CYS D 6
REMARK 465 ASN D 7
REMARK 465 PRO D 8
REMARK 465 ILE C 1
REMARK 465 TRP C 2
REMARK 465 GLY C 3
REMARK 465 ILE C 4
REMARK 465 GLY C 5
REMARK 465 CYS C 6
REMARK 465 ASN C 7
REMARK 465 PRO C 8
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 727 CG CD CE NZ
REMARK 470 LYS B 727 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 913 O HOH A 1526 1.51
REMARK 500 O HOH A 1207 O HOH A 1541 1.55
REMARK 500 O ALA A 490 O HOH A 801 1.65
REMARK 500 O HOH B 813 O HOH B 1576 1.68
REMARK 500 O HOH A 816 O HOH A 1207 1.70
REMARK 500 O HOH A 805 O HOH A 1361 1.74
REMARK 500 O HOH B 1514 O HOH B 1664 1.81
REMARK 500 O HOH B 806 O HOH B 1395 1.81
REMARK 500 O HOH B 838 O HOH B 885 1.84
REMARK 500 O HOH B 848 O HOH B 1046 1.84
REMARK 500 O HOH B 806 O HOH B 1069 1.90
REMARK 500 O TRP C 9 O HOH C 101 1.91
REMARK 500 O HOH A 893 O HOH A 931 1.91
REMARK 500 O HOH A 1547 O HOH A 1586 1.94
REMARK 500 O HOH A 965 O HOH A 1637 1.95
REMARK 500 O HOH A 1587 O HOH A 1670 1.95
REMARK 500 NE2 GLN A 24 O HOH A 802 1.96
REMARK 500 O HOH A 852 O HOH A 1669 1.99
REMARK 500 O HOH A 1249 O HOH A 1570 1.99
REMARK 500 O HOH B 829 O HOH B 1464 2.00
REMARK 500 O HOH A 837 O HOH A 880 2.01
REMARK 500 O HOH B 1232 O HOH B 1643 2.01
REMARK 500 O HOH A 1268 O HOH A 1637 2.02
REMARK 500 O HOH B 1383 O HOH B 1542 2.05
REMARK 500 O HOH B 1393 O HOH B 1706 2.05
REMARK 500 OE2 GLU B 247 O HOH B 801 2.06
REMARK 500 O LYS A 727 O HOH A 803 2.07
REMARK 500 O HOH B 1250 O HOH B 1280 2.08
REMARK 500 O HOH C 104 O HOH C 117 2.08
REMARK 500 O HOH C 112 O HOH C 122 2.08
REMARK 500 O HOH A 956 O HOH D 121 2.08
REMARK 500 O HOH B 826 O HOH B 1588 2.09
REMARK 500 O HOH B 941 O HOH B 1646 2.10
REMARK 500 O HOH B 813 O HOH B 1667 2.10
REMARK 500 NE2 GLN A 38 O HOH A 804 2.11
REMARK 500 OE1 GLN B 187 O HOH B 802 2.12
REMARK 500 NH1 ARG A 224 O HOH A 805 2.12
REMARK 500 OE1 GLU B 268 O HOH B 803 2.12
REMARK 500 O HOH A 1527 O HOH A 1669 2.13
REMARK 500 N ILE A 521 O HOH A 801 2.13
REMARK 500 O HOH B 1392 O HOH B 1460 2.13
REMARK 500 O HOH A 810 O HOH A 981 2.15
REMARK 500 O THR A 281 O HOH A 806 2.15
REMARK 500 O HOH A 811 O HOH A 1152 2.16
REMARK 500 O HOH A 1594 O HOH A 1623 2.16
REMARK 500 O HOH A 1537 O HOH D 117 2.16
REMARK 500 NE2 GLN A 187 O HOH A 807 2.18
REMARK 500 O HOH B 827 O HOH B 1497 2.18
REMARK 500 O HOH A 837 O HOH A 1250 2.18
REMARK 500 O HOH B 1632 O HOH B 1643 2.19
REMARK 500
REMARK 500 THIS ENTRY HAS 54 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 840 O HOH B 1643 3555 1.88
REMARK 500 O HOH A 1668 O HOH B 1132 4455 1.95
REMARK 500 O HOH A 1523 O HOH B 1608 3655 2.00
REMARK 500 O HOH A 1622 O HOH B 1308 3555 2.12
REMARK 500 O HOH A 1609 O HOH B 1433 3555 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 535 CB GLU A 535 CG 0.119
REMARK 500 TRP B 6 CB TRP B 6 CG 0.120
REMARK 500 SER B 282 N SER B 282 CA -0.163
REMARK 500 LYS B 570 CA LYS B 570 C 0.160
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 111 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 350 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET B 145 CG - SD - CE ANGL. DEV. = 11.2 DEGREES
REMARK 500 SER B 282 N - CA - C ANGL. DEV. = -18.9 DEGREES
REMARK 500 ARG B 378 C - N - CA ANGL. DEV. = 15.4 DEGREES
REMARK 500 ARG B 378 O - C - N ANGL. DEV. = 10.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 280 -166.58 -167.49
REMARK 500 LYS A 283 40.53 -84.04
REMARK 500 ALA A 311 -26.96 -148.98
REMARK 500 ALA A 332 77.70 -162.92
REMARK 500 TYR A 335 162.27 73.51
REMARK 500 GLU A 369 -37.53 68.76
REMARK 500 GLU A 452 -55.66 72.68
REMARK 500 TYR A 496 -70.95 -124.85
REMARK 500 ARG A 543 -120.72 53.87
REMARK 500 ALA A 577 -119.30 64.23
REMARK 500 ALA A 605 -24.99 -149.11
REMARK 500 THR A 614 -116.30 33.36
REMARK 500 ASP B 280 -162.18 -165.73
REMARK 500 ALA B 311 -27.13 -149.48
REMARK 500 ALA B 332 79.48 -161.63
REMARK 500 TYR B 335 162.22 71.82
REMARK 500 GLU B 369 -36.64 69.58
REMARK 500 GLU B 452 -55.56 73.99
REMARK 500 TYR B 496 -70.14 -124.68
REMARK 500 ARG B 543 -120.38 54.05
REMARK 500 ALA B 577 -119.39 63.29
REMARK 500 ALA B 605 -26.02 -148.17
REMARK 500 THR B 614 -115.19 34.58
REMARK 500 ASP D 23 54.26 -149.00
REMARK 500 ASP C 23 53.77 -147.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1754 DISTANCE = 5.83 ANGSTROMS
DBREF 5N4B A 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4B B 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4B D 1 25 UNP H2E7Q5 H2E7Q5_9AGAR 11 35
DBREF 5N4B C 1 25 UNP H2E7Q5 H2E7Q5_9AGAR 11 35
SEQADV 5N4B GLY A 0 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4B ALA A 577 UNP H2E7Q8 SER 577 ENGINEERED MUTATION
SEQADV 5N4B GLY B 0 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4B ALA B 577 UNP H2E7Q8 SER 577 ENGINEERED MUTATION
SEQRES 1 A 731 GLY MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO
SEQRES 2 A 731 SER THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER
SEQRES 3 A 731 ALA SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN
SEQRES 4 A 731 TRP LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR
SEQRES 5 A 731 THR ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN
SEQRES 6 A 731 ASN ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA
SEQRES 7 A 731 SER ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU
SEQRES 8 A 731 ASP ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU
SEQRES 9 A 731 GLN SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA
SEQRES 10 A 731 LEU PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP
SEQRES 11 A 731 VAL PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER
SEQRES 12 A 731 ALA GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS
SEQRES 13 A 731 PHE PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR
SEQRES 14 A 731 SER THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER
SEQRES 15 A 731 GLN ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER
SEQRES 16 A 731 ASP GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP
SEQRES 17 A 731 THR LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO
SEQRES 18 A 731 ALA ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN
SEQRES 19 A 731 ALA MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU
SEQRES 20 A 731 GLU ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU
SEQRES 21 A 731 TRP ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR
SEQRES 22 A 731 LEU TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN
SEQRES 23 A 731 LEU LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS
SEQRES 24 A 731 SER GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA
SEQRES 25 A 731 ALA ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL
SEQRES 26 A 731 TYR ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL
SEQRES 27 A 731 ILE THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG
SEQRES 28 A 731 ASP PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN
SEQRES 29 A 731 VAL ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR
SEQRES 30 A 731 LYS ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS
SEQRES 31 A 731 ALA GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL
SEQRES 32 A 731 GLY ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS
SEQRES 33 A 731 PHE PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR
SEQRES 34 A 731 ILE ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG
SEQRES 35 A 731 PHE SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP
SEQRES 36 A 731 PRO ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER
SEQRES 37 A 731 LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS
SEQRES 38 A 731 LYS SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN
SEQRES 39 A 731 TYR GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE
SEQRES 40 A 731 PHE SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY
SEQRES 41 A 731 ALA ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU
SEQRES 42 A 731 PHE GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR
SEQRES 43 A 731 LYS VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN
SEQRES 44 A 731 PHE LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL
SEQRES 45 A 731 ALA ILE ASN GLY ALA ALA ASN GLY GLY LEU LEU VAL MET
SEQRES 46 A 731 GLY SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA
SEQRES 47 A 731 ALA VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE
SEQRES 48 A 731 HIS LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR
SEQRES 49 A 731 GLY ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR
SEQRES 50 A 731 PRO LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL
SEQRES 51 A 731 MET PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY
SEQRES 52 A 731 ARG VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR
SEQRES 53 A 731 LEU GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU
SEQRES 54 A 731 ILE LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY
SEQRES 55 A 731 LYS PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS
SEQRES 56 A 731 TRP GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS
SEQRES 57 A 731 THR VAL GLU
SEQRES 1 B 731 GLY MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO
SEQRES 2 B 731 SER THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER
SEQRES 3 B 731 ALA SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN
SEQRES 4 B 731 TRP LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR
SEQRES 5 B 731 THR ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN
SEQRES 6 B 731 ASN ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA
SEQRES 7 B 731 SER ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU
SEQRES 8 B 731 ASP ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU
SEQRES 9 B 731 GLN SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA
SEQRES 10 B 731 LEU PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP
SEQRES 11 B 731 VAL PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER
SEQRES 12 B 731 ALA GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS
SEQRES 13 B 731 PHE PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR
SEQRES 14 B 731 SER THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER
SEQRES 15 B 731 GLN ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER
SEQRES 16 B 731 ASP GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP
SEQRES 17 B 731 THR LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO
SEQRES 18 B 731 ALA ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN
SEQRES 19 B 731 ALA MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU
SEQRES 20 B 731 GLU ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU
SEQRES 21 B 731 TRP ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR
SEQRES 22 B 731 LEU TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN
SEQRES 23 B 731 LEU LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS
SEQRES 24 B 731 SER GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA
SEQRES 25 B 731 ALA ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL
SEQRES 26 B 731 TYR ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL
SEQRES 27 B 731 ILE THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG
SEQRES 28 B 731 ASP PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN
SEQRES 29 B 731 VAL ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR
SEQRES 30 B 731 LYS ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS
SEQRES 31 B 731 ALA GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL
SEQRES 32 B 731 GLY ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS
SEQRES 33 B 731 PHE PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR
SEQRES 34 B 731 ILE ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG
SEQRES 35 B 731 PHE SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP
SEQRES 36 B 731 PRO ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER
SEQRES 37 B 731 LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS
SEQRES 38 B 731 LYS SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN
SEQRES 39 B 731 TYR GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE
SEQRES 40 B 731 PHE SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY
SEQRES 41 B 731 ALA ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU
SEQRES 42 B 731 PHE GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR
SEQRES 43 B 731 LYS VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN
SEQRES 44 B 731 PHE LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL
SEQRES 45 B 731 ALA ILE ASN GLY ALA ALA ASN GLY GLY LEU LEU VAL MET
SEQRES 46 B 731 GLY SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA
SEQRES 47 B 731 ALA VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE
SEQRES 48 B 731 HIS LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR
SEQRES 49 B 731 GLY ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR
SEQRES 50 B 731 PRO LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL
SEQRES 51 B 731 MET PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY
SEQRES 52 B 731 ARG VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR
SEQRES 53 B 731 LEU GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU
SEQRES 54 B 731 ILE LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY
SEQRES 55 B 731 LYS PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS
SEQRES 56 B 731 TRP GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS
SEQRES 57 B 731 THR VAL GLU
SEQRES 1 D 25 ILE TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS
SEQRES 2 D 25 VAL ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS
SEQRES 1 C 25 ILE TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS
SEQRES 2 C 25 VAL ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS
FORMUL 5 HOH *1941(H2 O)
HELIX 1 AA1 TYR A 37 GLU A 42 5 6
HELIX 2 AA2 THR A 44 GLN A 64 1 21
HELIX 3 AA3 ALA A 66 ASN A 80 1 15
HELIX 4 AA4 ASP A 119 LYS A 122 5 4
HELIX 5 AA5 GLY A 123 VAL A 127 1 5
HELIX 6 AA6 ASP A 133 LEU A 137 5 5
HELIX 7 AA7 SER A 181 GLY A 188 1 8
HELIX 8 AA8 THR A 244 ASP A 248 5 5
HELIX 9 AA9 ASP A 454 ASP A 456 5 3
HELIX 10 AB1 SER A 508 GLY A 519 1 12
HELIX 11 AB2 GLY A 534 GLY A 540 1 7
HELIX 12 AB3 GLY A 541 THR A 545 5 5
HELIX 13 AB4 LYS A 546 ASN A 563 1 18
HELIX 14 AB5 ALA A 577 ALA A 590 1 14
HELIX 15 AB6 LYS A 609 PHE A 613 5 5
HELIX 16 AB7 GLY A 615 ALA A 618 5 4
HELIX 17 AB8 TRP A 619 GLY A 624 1 6
HELIX 18 AB9 ILE A 628 TYR A 636 1 9
HELIX 19 AC1 SER A 639 ASN A 643 5 5
HELIX 20 AC2 PRO A 666 VAL A 680 1 15
HELIX 21 AC3 PRO A 703 LEU A 722 1 20
HELIX 22 AC4 TYR B 37 GLU B 42 5 6
HELIX 23 AC5 THR B 44 GLN B 64 1 21
HELIX 24 AC6 ALA B 66 ASN B 80 1 15
HELIX 25 AC7 ASP B 119 LYS B 122 5 4
HELIX 26 AC8 GLY B 123 VAL B 127 1 5
HELIX 27 AC9 ASP B 133 LEU B 137 5 5
HELIX 28 AD1 SER B 181 GLY B 188 1 8
HELIX 29 AD2 THR B 244 ASP B 248 5 5
HELIX 30 AD3 ASP B 454 ASP B 456 5 3
HELIX 31 AD4 SER B 508 GLY B 519 1 12
HELIX 32 AD5 GLY B 534 GLY B 540 1 7
HELIX 33 AD6 GLY B 541 THR B 545 5 5
HELIX 34 AD7 LYS B 546 ASN B 563 1 18
HELIX 35 AD8 ALA B 577 ALA B 590 1 14
HELIX 36 AD9 LYS B 609 PHE B 613 5 5
HELIX 37 AE1 GLY B 615 ALA B 618 5 4
HELIX 38 AE2 TRP B 619 GLY B 624 1 6
HELIX 39 AE3 ILE B 628 TYR B 636 1 9
HELIX 40 AE4 PRO B 637 ASN B 643 5 7
HELIX 41 AE5 PRO B 666 VAL B 680 1 15
HELIX 42 AE6 PRO B 703 LEU B 722 1 20
SHEET 1 AA1 2 VAL A 20 SER A 25 0
SHEET 2 AA1 2 GLY A 29 PRO A 34 -1 O VAL A 33 N ASP A 21
SHEET 1 AA2 3 LYS A 83 PHE A 84 0
SHEET 2 AA2 3 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA2 3 THR A 88 LEU A 89 -1 N THR A 88 O TYR A 96
SHEET 1 AA3 4 LYS A 83 PHE A 84 0
SHEET 2 AA3 4 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA3 4 VAL A 108 SER A 112 -1 O TYR A 110 N TRP A 97
SHEET 4 AA3 4 GLY A 128 PHE A 132 -1 O PHE A 131 N LEU A 109
SHEET 1 AA4 4 ALA A 143 PHE A 150 0
SHEET 2 AA4 4 PHE A 156 HIS A 163 -1 O ALA A 160 N LEU A 147
SHEET 3 AA4 4 SER A 169 SER A 175 -1 O THR A 170 N VAL A 161
SHEET 4 AA4 4 VAL A 197 PHE A 200 -1 O VAL A 197 N ILE A 171
SHEET 1 AA5 4 ILE A 206 TRP A 207 0
SHEET 2 AA5 4 GLY A 213 ARG A 218 -1 O LEU A 215 N ILE A 206
SHEET 3 AA5 4 MET A 235 LYS A 240 -1 O CYS A 237 N TYR A 216
SHEET 4 AA5 4 ILE A 249 GLN A 253 -1 O TYR A 252 N MET A 236
SHEET 1 AA6 4 ILE A 261 THR A 266 0
SHEET 2 AA6 4 TYR A 272 PHE A 278 -1 O TYR A 274 N ASP A 265
SHEET 3 AA6 4 LEU A 286 GLU A 291 -1 O ALA A 290 N LEU A 273
SHEET 4 AA6 4 ARG A 304 VAL A 307 -1 O VAL A 307 N LEU A 287
SHEET 1 AA7 4 TYR A 314 HIS A 320 0
SHEET 2 AA7 4 LEU A 323 THR A 328 -1 O TYR A 325 N ILE A 317
SHEET 3 AA7 4 LYS A 336 ASP A 341 -1 O ILE A 338 N ILE A 326
SHEET 4 AA7 4 GLU A 348 ILE A 353 -1 O PHE A 352 N VAL A 337
SHEET 1 AA8 4 LYS A 360 ALA A 367 0
SHEET 2 AA8 4 TYR A 371 ARG A 378 -1 O LYS A 377 N LYS A 360
SHEET 3 AA8 4 LYS A 381 TYR A 387 -1 O TYR A 387 N PHE A 372
SHEET 4 AA8 4 GLN A 393 LEU A 397 -1 O LEU A 394 N LEU A 386
SHEET 1 AA9 4 ALA A 404 ALA A 408 0
SHEET 2 AA9 4 HIS A 415 GLY A 422 -1 O PHE A 417 N ALA A 408
SHEET 3 AA9 4 THR A 425 ASP A 433 -1 O THR A 428 N LEU A 420
SHEET 4 AA9 4 PHE A 442 THR A 447 -1 O ARG A 446 N ILE A 429
SHEET 1 AB1 8 PHE A 458 GLU A 466 0
SHEET 2 AB1 8 LYS A 472 HIS A 480 -1 O ILE A 473 N TYR A 465
SHEET 3 AB1 8 ILE A 521 PRO A 525 -1 O PHE A 522 N VAL A 478
SHEET 4 AB1 8 ALA A 491 TYR A 494 1 N ILE A 492 O ALA A 523
SHEET 5 AB1 8 VAL A 571 ALA A 576 1 O ALA A 572 N GLN A 493
SHEET 6 AB1 8 ALA A 597 GLU A 601 1 O GLU A 601 N GLY A 575
SHEET 7 AB1 8 ALA A 652 ASN A 658 1 O LEU A 654 N ALA A 598
SHEET 8 AB1 8 LEU A 687 ASP A 692 1 O LYS A 690 N ILE A 655
SHEET 1 AB2 2 VAL B 20 SER B 25 0
SHEET 2 AB2 2 GLY B 29 PRO B 34 -1 O VAL B 33 N ASP B 21
SHEET 1 AB3 3 LYS B 83 PHE B 84 0
SHEET 2 AB3 3 TRP B 95 ASN B 100 -1 O ASN B 100 N LYS B 83
SHEET 3 AB3 3 THR B 88 LEU B 89 -1 N THR B 88 O TYR B 96
SHEET 1 AB4 4 LYS B 83 PHE B 84 0
SHEET 2 AB4 4 TRP B 95 ASN B 100 -1 O ASN B 100 N LYS B 83
SHEET 3 AB4 4 VAL B 108 SER B 112 -1 O TYR B 110 N TRP B 97
SHEET 4 AB4 4 GLY B 128 PHE B 132 -1 O PHE B 131 N LEU B 109
SHEET 1 AB5 4 ALA B 143 PHE B 150 0
SHEET 2 AB5 4 PHE B 156 HIS B 163 -1 O ALA B 160 N LEU B 147
SHEET 3 AB5 4 SER B 169 SER B 175 -1 O THR B 170 N VAL B 161
SHEET 4 AB5 4 VAL B 197 PHE B 200 -1 O VAL B 197 N ILE B 171
SHEET 1 AB6 4 ILE B 206 TRP B 207 0
SHEET 2 AB6 4 GLY B 213 ARG B 218 -1 O LEU B 215 N ILE B 206
SHEET 3 AB6 4 MET B 235 LYS B 240 -1 O HIS B 239 N PHE B 214
SHEET 4 AB6 4 ILE B 249 TYR B 252 -1 O TYR B 252 N MET B 236
SHEET 1 AB7 4 ILE B 261 THR B 266 0
SHEET 2 AB7 4 TYR B 272 PHE B 278 -1 O TYR B 274 N ASP B 265
SHEET 3 AB7 4 LEU B 286 GLU B 291 -1 O ALA B 290 N LEU B 273
SHEET 4 AB7 4 ARG B 304 VAL B 307 -1 O VAL B 307 N LEU B 287
SHEET 1 AB8 4 TYR B 314 HIS B 320 0
SHEET 2 AB8 4 LEU B 323 THR B 328 -1 O TYR B 325 N THR B 318
SHEET 3 AB8 4 LYS B 336 ASP B 341 -1 O ILE B 340 N VAL B 324
SHEET 4 AB8 4 ILE B 349 ILE B 353 -1 O PHE B 352 N VAL B 337
SHEET 1 AB9 4 LYS B 360 ALA B 367 0
SHEET 2 AB9 4 TYR B 371 ARG B 378 -1 O VAL B 373 N ASN B 365
SHEET 3 AB9 4 LYS B 381 TYR B 387 -1 O TYR B 387 N PHE B 372
SHEET 4 AB9 4 GLN B 393 LEU B 397 -1 O LEU B 394 N LEU B 386
SHEET 1 AC1 4 ALA B 404 ALA B 408 0
SHEET 2 AC1 4 HIS B 415 GLY B 422 -1 O SER B 421 N ALA B 404
SHEET 3 AC1 4 THR B 425 ASP B 433 -1 O THR B 428 N LEU B 420
SHEET 4 AC1 4 PHE B 442 THR B 447 -1 O ARG B 446 N ILE B 429
SHEET 1 AC2 8 PHE B 458 GLU B 466 0
SHEET 2 AC2 8 LYS B 472 HIS B 480 -1 O ILE B 473 N TYR B 465
SHEET 3 AC2 8 ILE B 521 PRO B 525 -1 O PHE B 522 N VAL B 478
SHEET 4 AC2 8 ALA B 491 TYR B 494 1 N ILE B 492 O ALA B 523
SHEET 5 AC2 8 VAL B 571 ALA B 576 1 O ALA B 572 N GLN B 493
SHEET 6 AC2 8 ALA B 597 GLU B 601 1 O GLU B 601 N GLY B 575
SHEET 7 AC2 8 ALA B 652 ASN B 658 1 O LEU B 654 N ALA B 598
SHEET 8 AC2 8 LEU B 687 ASP B 692 1 O LEU B 688 N THR B 653
CRYST1 99.084 114.716 141.265 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010092 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008717 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007079 0.00000
TER 5797 LYS A 727
TER 11595 LYS B 727
TER 11726 CYS D 25
TER 11857 CYS C 25
MASTER 651 0 0 42 82 0 0 613657 4 0 118
END |